IPPK_DROME
ID IPPK_DROME Reviewed; 621 AA.
AC Q9W2Q7; Q95R36;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Inositol-pentakisphosphate 2-kinase;
DE EC=2.7.1.158 {ECO:0000305|PubMed:15322119};
DE AltName: Full=Inositol-1,3,4,5,6-pentakisphosphate 2-kinase;
DE AltName: Full=Ins(1,3,4,5,6)P5 2-kinase;
DE Short=DmIpk1 {ECO:0000303|PubMed:15322119};
DE Short=InsP5 2-kinase;
GN Name=Ipk1; ORFNames=CG30295;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15322119; DOI=10.1074/jbc.m408295200;
RA Seeds A.M., Sandquist J.C., Spana E.P., York J.D.;
RT "A molecular basis for inositol polyphosphate synthesis in Drosophila
RT melanogaster.";
RL J. Biol. Chem. 279:47222-47232(2004).
CC -!- FUNCTION: Contributes to the formation of Ins(1,2,3,4,5,6)P6 (InsP6,
CC IP6 or phytate) (PubMed:15322119). Phosphorylates Ins(1,3,4,5,6)P5 at
CC position 2 to form InsP6 (Probable). Together with Ipk2, they are the
CC main contributors to higher InsP synthesis (PubMed:15322119).
CC {ECO:0000269|PubMed:15322119, ECO:0000303|PubMed:15322119,
CC ECO:0000305|PubMed:15322119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC Evidence={ECO:0000305|PubMed:15322119};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20314;
CC Evidence={ECO:0000305|PubMed:15322119};
CC -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC kinases of both family 1 and 2.
CC -!- SIMILARITY: Belongs to the IPK1 type 2 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF46633.2; -; Genomic_DNA.
DR EMBL; AY061821; AAL27632.1; -; mRNA.
DR RefSeq; NP_611522.1; NM_137678.3.
DR AlphaFoldDB; Q9W2Q7; -.
DR BioGRID; 63006; 1.
DR STRING; 7227.FBpp0112280; -.
DR PaxDb; Q9W2Q7; -.
DR DNASU; 37360; -.
DR EnsemblMetazoa; FBtr0071515; FBpp0071444; FBgn0050295.
DR GeneID; 37360; -.
DR KEGG; dme:Dmel_CG30295; -.
DR UCSC; CG30295-RA; d. melanogaster.
DR CTD; 37360; -.
DR FlyBase; FBgn0050295; Ipk1.
DR VEuPathDB; VectorBase:FBgn0050295; -.
DR eggNOG; KOG4749; Eukaryota.
DR GeneTree; ENSGT00390000010053; -.
DR InParanoid; Q9W2Q7; -.
DR Reactome; R-DME-1855167; Synthesis of pyrophosphates in the cytosol.
DR Reactome; R-DME-1855191; Synthesis of IPs in the nucleus.
DR BioGRID-ORCS; 37360; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37360; -.
DR PRO; PR:Q9W2Q7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0050295; Expressed in cleaving embryo and 14 other tissues.
DR ExpressionAtlas; Q9W2Q7; baseline and differential.
DR Genevisible; Q9W2Q7; DM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IMP:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:FlyBase.
DR GO; GO:0052746; P:inositol phosphorylation; IMP:UniProtKB.
DR Gene3D; 3.30.200.110; -; 1.
DR InterPro; IPR009286; Ins_P5_2-kin.
DR InterPro; IPR043001; IP5_2-K_N_lobe.
DR PANTHER; PTHR14456; PTHR14456; 1.
DR Pfam; PF06090; Ins_P5_2-kin; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..621
FT /note="Inositol-pentakisphosphate 2-kinase"
FT /id="PRO_0000110533"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 241..245
FT /note="EXKPK motif"
FT COMPBIAS 396..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 67447 MW; 749B39BDCEC1EB53 CRC64;
MTAERGPRSP GTGQKLRLRA TEPMPQWTAK NLHALLDLPA AMELRQIELI YRAEGNANLV
LALPQFKKVL RLPKMISSRL RQAAHQRHEL ADEVARPEGQ RVSSERAGTE NAGDLTMPDF
MAYIGIMRRL LGNEFVCGAD IVAIPKEDDR FWINEHIRAQ RPVSRLDKEF VGPFGLLLPD
VTQLPATFDV LLANLQAKGT TGDESGAAAG VGDGGGVGRG AGTRTKNRSA VRRLGDTYAI
EIKPKQGWLQ LASDVNDLFD LMPSGAVTKP KETTCNQEEN EPSARDKCWC RFCSMQLLKM
HNGKIKRLGH YCPLDLFSGT PSRMLDALDA LLACPQNNLR VFQNSNLIYG DHANSISFDE
LSSRVFPGEI MVLIKHLLVA CLLREYEHPE SKRAEGSNQS QKQQQEQPEP EQLNQSRVSI
AATETKAGAA GIGAANVVLP LGGRAAAPVV TAGQSSTRTR AAAATATTQR YTKVARVETT
ITRQAATSMA AGPASSSQLS GNVLATATAT ATATAMATSG RTETKTEPET PAEAASTTSR
NVNQNESQKL NRNEPANQTQ AQNNKTEIFR LPKNCVLQKI LNLQLLVKVS QPIKLLPKLL
SLCPFGFVYS ACPPENLGNC R
